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5iqn
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the E. coli type 1 pilus subunit FimG (engineered variant with substitution Q134E; N-terminal FimG residues 1-12 truncated) in complex with the donor strand peptide DsF_SRIRIRGYVR== | |
| + | <StructureSection load='5iqn' size='340' side='right' caption='[[5iqn]], [[Resolution|resolution]] 1.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5iqn]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IQN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IQN FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5iqn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iqn OCA], [http://pdbe.org/5iqn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5iqn RCSB], [http://www.ebi.ac.uk/pdbsum/5iqn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5iqn ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/FIMG_ECOLI FIMG_ECOLI]] Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Involved in the integration of FimH in the fimbriae. [[http://www.uniprot.org/uniprot/FIMF_ECOLI FIMF_ECOLI]] Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Involved in the integration of FimH in the fimbriae. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The complex between the bacterial type 1 pilus subunit FimG and the peptide corresponding to the N-terminal extension (termed donor strand, Ds) of the partner subunit FimF (DsF) shows the strongest reported noncovalent molecular interaction, with a dissociation constant (KD ) of 1.5x10-20 m. However, the complex only exhibits a slow association rate of 330 m-1 s-1 that limits technical applications, such as its use in affinity purification. Herein, a structure-based approach was used to design pairs of FimGt (a FimG variant lacking its own N-terminal extension) and DsF variants with enhanced electrostatic surface complementarity. Association of the best mutant FimGt/DsF pairs was accelerated by more than two orders of magnitude, while the dissociation rates and 3D structures of the improved complexes remained essentially unperturbed. A KD value of 8.8x10-22 m was obtained for the best mutant complex, which is the lowest value reported to date for a protein/ligand complex. | ||
| - | + | Accelerating the Association of the Most Stable Protein-Ligand Complex by more than Two Orders of Magnitude.,Giese C, Eras J, Kern A, Scharer MA, Capitani G, Glockshuber R Angew Chem Int Ed Engl. 2016 Jun 28. doi: 10.1002/anie.201603652. PMID:27351462<ref>PMID:27351462</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5iqn" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Capitani, G]] | ||
[[Category: Eras, J]] | [[Category: Eras, J]] | ||
| - | [[Category: Scharer, M.A]] | ||
| - | [[Category: Kern, A]] | ||
| - | [[Category: Glockshuber, R]] | ||
[[Category: Giese, C]] | [[Category: Giese, C]] | ||
| - | [[Category: | + | [[Category: Glockshuber, R]] |
| + | [[Category: Kern, A]] | ||
| + | [[Category: Scharer, M A]] | ||
| + | [[Category: Cell adhesion]] | ||
| + | [[Category: Complex]] | ||
| + | [[Category: Fimgt]] | ||
| + | [[Category: Protein]] | ||
Revision as of 02:21, 13 July 2016
Crystal structure of the E. coli type 1 pilus subunit FimG (engineered variant with substitution Q134E; N-terminal FimG residues 1-12 truncated) in complex with the donor strand peptide DsF_SRIRIRGYVR
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Categories: Capitani, G | Eras, J | Giese, C | Glockshuber, R | Kern, A | Scharer, M A | Cell adhesion | Complex | Fimgt | Protein
